Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

Kalvis Brangulis (Coresponding Author), Inara Akopjana, Ivars Petrovskis, Andris Kazaks, Atis Jēkabsons, Kristaps Jaudzems, Artūrs Vīksna, Māris Bērtiņš, Kaspars Tars

Research output: Contribution to journalArticlepeer-review

Abstract

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+-binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.

Original languageEnglish
Pages (from-to)317-326
Number of pages10
JournalFEBS Letters
Volume594
Issue number2
DOIs
Publication statusPublished - 1 Jan 2020
Externally publishedYes

Keywords

  • Ixodes ticks
  • Lyme borreliosis
  • Lyme disease
  • metalloenzyme
  • spirochete

Field of Science

  • 3.1 Basic medicine
  • 1.6 Biological sciences

Publication Type

  • 1.1. Scientific article indexed in Web of Science and/or Scopus database

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